Isolation, cDNA Cloning, Biological Properties, and Carbohydrate Binding Specificity of Sieboldin-b, a Type II Ribosome-Inactivating Protein from the Bark of Japanese Elderberry (Sambucus sieboldiana)

1997 ◽  
Vol 340 (2) ◽  
pp. 185-194 ◽  
Author(s):  
Maria Angeles Rojo ◽  
Misa Yato ◽  
Naoko Ishii-Minami ◽  
Eiichi Minami ◽  
Hanae Kaku ◽  
...  
Keyword(s):  
Cdna Cloning ◽  
Binding Specificity ◽  
Biological Properties ◽  
Carbohydrate Binding ◽  
Type Ii ◽  
Ribosome Inactivating Protein

scholarly journals Biochemical and structural characterization of the novel sialic acid-binding site of Escherichia coli heat-labile enterotoxin LT-IIb

2016 ◽  
Vol 473 (21) ◽  
pp. 3923-3936 ◽  
Author(s):  
Dani Zalem ◽  
João P. Ribeiro ◽  
Annabelle Varrot ◽  
Michael Lebens ◽  
Anne Imberty ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Cholera Toxin ◽  
Carbohydrate Binding ◽  
Type I ◽  
Type Ii ◽  
E Coli ◽  
B Subunit ◽  
Heat Labile ◽  
B Subunits

The structurally related AB5-type heat-labile enterotoxins of Escherichia coli and Vibrio cholerae are classified into two major types. The type I group includes cholera toxin (CT) and E. coli LT-I, whereas the type II subfamily comprises LT-IIa, LT-IIb and LT-IIc. The carbohydrate-binding specificities of LT-IIa, LT-IIb and LT-IIc are distinctive from those of cholera toxin and E. coli LT-I. Whereas CT and LT-I bind primarily to the GM1 ganglioside, LT-IIa binds to gangliosides GD1a, GD1b and GM1, LT-IIb binds to the GD1a and GT1b gangliosides, and LT-IIc binds to GM1, GM2, GM3 and GD1a. These previous studies of the binding properties of type II B-subunits have been focused on ganglio core chain gangliosides. To further define the carbohydrate binding specificity of LT-IIb B-subunits, we have investigated its binding to a collection of gangliosides and non-acid glycosphingolipids with different core chains. A high-affinity binding of LT-IIb B-subunits to gangliosides with a neolacto core chain, such as Neu5Gcα3- and Neu5Acα3-neolactohexaosylceramide, and Neu5Gcα3- and Neu5Acα3-neolactooctaosylceramide was detected. An LT-IIb-binding ganglioside was isolated from human small intestine and characterized as Neu5Acα3-neolactohexaosylceramide. The crystal structure of the B-subunit of LT-IIb with the pentasaccharide moiety of Neu5Acα3-neolactotetraosylceramide (Neu5Ac-nLT: Neu5Acα3Galβ4GlcNAcβ3Galβ4Glc) was determined providing the first information for a sialic-binding site in this subfamily, with clear differences from that of CT and LT-I.

scholarly journals Carbohydrate binding specificity of immobilized Psathyrella velutina lectin.

1992 ◽  
Vol 267 (2) ◽  
pp. 707-713
Author(s):  
T Endo ◽  
H Ohbayashi ◽  
K Kanazawa ◽  
N Kochibe ◽  
A Kobata
Keyword(s):  
Binding Specificity ◽  
Carbohydrate Binding

scholarly journals cDNA Cloning and Characterization of Type II Procollagen α1 Chain in the Skate Raja kenojei

2006 ◽  
Vol 9 (1) ◽  
pp. 22-29
Author(s):  
Jae-Ho Hwang ◽  
Yoshihiro Yokoyama ◽  
Shoshi Mizuta ◽  
Reiji Yoshinaka
Keyword(s):  
Cdna Cloning ◽  
Type Ii

scholarly journals Carbohydrate/glycan-binding specificity of legume lectins in respect to their proposed biological functions

2000 ◽  
Vol 43 (4) ◽  
pp. 349-359 ◽  
Author(s):  
Márcio Viana Ramos ◽  
Thalles Barbosa Grangeiro ◽  
Benildo Sousa Cavada ◽  
Iain Shepherd ◽  
Roberval Oliveira de Melo Lopes ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Binding Specificity ◽  
Biological Properties ◽  
The Other ◽  
Biological Functions ◽  
Main Hypothesis ◽  
Physiological Functions ◽  
Legume Plants ◽  
Legume Lectins ◽  
Structural Aspects

The lectins, proteins which specifically recognize carbohydrate moieties, have been extensively studied in many biochemical and structural aspects in order to establish the molecular basis of this non-catalytic event. On the other hand, their clinical and agricultural potentials have been growing fast. Although lectins, mainly those from legume plants, had been investigated for biological properties, studies about the physiological functions of lectins are scarce in literature. Therefore, despite the accumulated data on lectins (as proteins), the role played by these signalizing molecules is poorly discussed. In the light of our accumulated results on legume lectins, specially those obtained from plants belonging to the Diocleinae sub-tribe and available data in literature, we discuss here the main hypothesis of their functions according to their carbohydrate/glycan-binding specificity.

scholarly journals Redefinition of the Carbohydrate Binding Specificity ofHelicobacter pyloriBabA Adhesin

2012 ◽  
Vol 287 (38) ◽  
pp. 31712-31724 ◽  
Author(s):  
John Benktander ◽  
Jonas Ångström ◽  
Michael E. Breimer ◽  
Susann Teneberg
Keyword(s):  
Binding Specificity ◽  
Carbohydrate Binding

cDNA Cloning and Genomic Organization of the Mouse BMP Type II Receptor

1997 ◽  
Vol 235 (3) ◽  
pp. 499-504 ◽  
Author(s):  
Hideyuki Beppu ◽  
Osamu Minowa ◽  
Kohei Miyazono ◽  
Masahiro Kawabata
Keyword(s):  
Cdna Cloning ◽  
Genomic Organization ◽  
Type Ii
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